Banerjee, U C (1993) Characterization of soluble rifamycin oxidase from Curvularia lunata var. aeria. Letters in applied microbiology, 17 (1). pp. 1-3. ISSN 0266-8254

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Abstract

Curvularia lunata var. aeria was grown on yeast extract, peptone and carboxymethylcellulose (YPC) medium for the production of extracellular rifamycin oxidase. The enzyme was partially purified through a Sephadex G-75 column. The half lives of rifamycin oxidase at 30 degrees and 40 degrees C were 9 d and 100 min, respectively. The activation and deactivation energies of the partially purified enzyme, calculated from Arrhenius plots, were 5.80 and 35.10 kcal mol-1, respectively. The enzyme exhibited a Km (rifamycin B) value of 0.67 mmol l-1 and a Vmax of 11 mumol h-1.ml. Three metal ions, Fe2+, Ag+ and Hg2+, inhibited the enzyme in the 10-20 mmol l-1 metal ion concentration range. Catalytic activity was not affected by the chelating agent, EDTA.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Wiley/ Blackwell
Subjects:	Q Science > QR Microbiology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	12 Dec 2011 15:37
Last Modified:	28 Mar 2014 11:06
URI:	http://crdd.osdd.net/open/id/eprint/418

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